A carboxy-terminal domain of Tir from enterohemorrhagic Escherichia coli O157:H7 (EHEC O157:H7) required for efficient type III secretion
A carboxy-terminal domain of Tir from enterohemorrhagic Escherichia coli O157:H7 (EHEC O157:H7) required for efficient type III secretion
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DOI：
10.1016/j.femsle.2004.12.027
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发表时间：
2005-02-15
影响因子：
2.1
通讯作者：
DeVinney, R
中科院分区：
文献类型：
--
作者：
Allen-Vercoe, E;Toh, MCW;DeVinney, R
肠出血性大肠杆菌（EHEC O157:H7）的III型分泌蛋白Tir在感染期间的粘附和基台形成中起核心作用。对于氨基末端外的Tir结构域如何促进有效的Tir分泌和易位，我们知之甚少。我们发现了一个6个氨基酸（519-524）的羧基末端区域，这是有效分泌和转运Tir所必需的。有趣的是，EHEC O157:H7 TirDelta519-524在相关致病性大肠杆菌中表达时能有效分泌。这些数据表明，该区域可能在维持EHEC O157:H7 Tir处于分泌能力构象中发挥作用。(C) 2004年欧洲微生物学会联合会。Elsevier B.V.版权所有。
The type III secreted protein Tir from Enterohemorrhagic Escherichia coli (EHEC O157:H7) plays a central role in adherence and pedestal formation during infection. Little is known about how Tir domains outside of the amino-terminus contribute to efficient Tir secretion and translocation. We found a 6 amino acid (519-524) carboxy-terminal region which was required for efficient Tir secretion and translocation. Interestingly, EHEC O157:H7 TirDelta519-524 was efficiently secreted when expressed in the related pathogen enteropathogenic E. coli. These data suggest that this region may play a role in maintaining EHEC O157:H7 Tir in a secretion-competent conformation. (C) 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.